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Crystals 2018, 8(2), 97;

Crystal Structure of Shigella flexneri SF173 Reveals a Dimeric Helical Bundle Conformation

College of Pharmacy, Chungbuk National University, Cheongju 28160, Chungbuk, Korea
Department of Biotechnology, College of Biomedical and Health Science, Konkuk University, Chungbuk 27478, Korea
Department of Molecular Science and Technology, Ajou University, Suwon 16499, Korea
Research Institute of Pharmaceutical Sciences and Technology (RIPST), College of Pharmacy, Ajou University, Suwon 16499, Korea
These authors contributed equally to this work.
Author to whom correspondence should be addressed.
Received: 29 December 2017 / Revised: 12 February 2018 / Accepted: 12 February 2018 / Published: 14 February 2018
(This article belongs to the Special Issue Recent Advances in Protein Crystallography)
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We report the crystal structure and bioinformatic analysis of SF173, a functionally uncharacterized protein from the human enteropathogenic bacteria Shigella flexneri. The structure shows a tightly interlinked dimer formed by adimeric core comprising α2 and α3 helices from both subunits and swapping the N-terminal α1 helix of each monomer. Structural inspection and genomic analysis results suggest that the SF173 might play its putative function by binding to SF172, the partially overlapped upstream product in the operon. As YaeO (an SF172 orthologue) has been identified to be an inhibitor of the bacterial transcription terminator Rho protein, SF173 is suggested to be involved in the regulation of Rho-dependent transcription termination, by inhibiting the Rho protein binding to SF172/YaeO. View Full-Text
Keywords: Shigella flexneri; SF173; X-ray crystallography; helical bundle Shigella flexneri; SF173; X-ray crystallography; helical bundle

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Kim, J.-H.; Won, H.-S.; Yoon, W.-S.; Seok, S.-H.; Jung, B.-J.; Lee, S.-N.; Sim, D.-W.; Seo, M.-D. Crystal Structure of Shigella flexneri SF173 Reveals a Dimeric Helical Bundle Conformation. Crystals 2018, 8, 97.

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